Exploring the binding mechanism of phosphoramidate derivative with DNA: Spectroscopy, calorimetry and modeling
Gongke Wang a, Hongwei Wu b, Dongchao Wang a, Changling Yan a, Yan Lu a,⇑
- School of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, Henan 453007, PR China
- Department of Chemistry, School of Basic Medicine, Xinxiang Medical University, Xinxiang, Henan 453003, PR China
" Medically important phosphoramidate derivative HMPAP is synthesized.
" HMPAP is intercalative binding into ctDNA helix.
" Hydrogen bonding may play an essential role in the binding of HMPAP with ctDNA.
" This binding interaction is
predominantly enthalpy driven.
a r t i c l e i n f o
- Article history:
- Received 29 June 2012
- Received in revised form 11 November 2012
- Accepted 16 November 2012
- Available online 5 December 2012
a b s t r a c t
In this study, one of the amino phosphine ester derivatives a-(3-hydroxy-4-methoxyphenyl)-N-phenyl- a-aminophosphonate (HMPAP) was synthesized, and the molecular interaction of HMPAP with ct-DNA has been investigated by UV–Vis absorption spectra, fluorescence spectra, isothermal titration calorime-try (ITC) and molecular modeling. The binding constant (Kb) of HMPAP to ct-DNA at different tempera- tures were calculated from fluorescence spectra. According to the UV–Vis absorption spectra, ethidium bromide displacement studies and ITC experimental results, we can conclude that HMPAP is an interca- lator. The molecular modeling results indicated that HMPAP can slide into the G–C rich region of ct-DNA. ITC data showed that ct-DNA/HMPAP binding is enthalpy controlled. Furthermore, the results obtained from molecular modeling corroborated the experimental results obtanied from spectroscopic and ITC investigations.
2012 Elsevier B.V. All rights reserved.
Keywords:
Amino phosphine ester derivative
DNA Intercalation Spectroscopy
Isothermal titration calorimetry
Molecular modeling
Full Pdf Download [In Here]
Baca Juga
Free Journal of - Determination of the thermodynamics of carbonic anhydrase acid-unfolding by titration calorimetry
Tag :
Physical Chemistry
0 Komentar untuk "Free Journal of - Exploring the binding mechanism of phosphoramidate derivative with DNA: Spectroscopy, calorimetry and modeling"